Caseinolytic mitochondrial matrix peptidase chaperone subunit X
mammalian protein found in Homo sapiens
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Caseinolytic mitochondrial matrix peptidase chaperone subunit X
Summary
Caseinolytic mitochondrial matrix peptidase chaperone subunit X is a protein[1]. It draws 38 Wikipedia views per month (protein category, ranking #153 of 987).[2]
Key Facts
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's instance of is recorded as protein[3].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X is part of Clp protease, ATP-binding subunit ClpX[4].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X is part of P-loop containing nucleoside triphosphate hydrolase[5].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X is part of Clp ATPase, C-terminal domain, protein family[6].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X is part of ATPase, AAA-type, core domain, protein family[7].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X is part of AAA proteins[8].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X comprises Clp ATPase, C-terminal[9].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X comprises AAA+ ATPase domain[10].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X comprises ATPase, AAA-type, core[11].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's molecular function is recorded as unfolded protein binding[12].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's molecular function is recorded as nucleotide binding[13].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's molecular function is recorded as protein binding[14].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's molecular function is recorded as peptidase activator activity[15].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's molecular function is recorded as metal ion binding[16].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's molecular function is recorded as ATP-dependent peptidase activity[17].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's molecular function is recorded as ATPase activity[18].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's molecular function is recorded as ATP binding[19].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's molecular function is recorded as ATP-dependent peptidase activity[20].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's cell component is recorded as mitochondrial endopeptidase Clp complex[21].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's cell component is recorded as mitochondrial matrix[22].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's cell component is recorded as nucleoplasm[23].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's cell component is recorded as endopeptidase Clp complex[24].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's cell component is recorded as mitochondrial nucleoid[25].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's cell component is recorded as mitochondrion[26].
- Caseinolytic mitochondrial matrix peptidase chaperone subunit X's cell component is recorded as cytosol[27].
Why It Matters
Caseinolytic mitochondrial matrix peptidase chaperone subunit X draws 38 Wikipedia views per month (protein category, ranking #153 of 987).[2] It is known by 5 alternative names across languages and contexts.[28]